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Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism.
Lee, Byung-Gil; Merkel, Fabian; Allegretti, Matteo; Hassler, Markus; Cawood, Christopher; Lecomte, Léa; O'Reilly, Francis J; Sinn, Ludwig R; Gutierrez-Escribano, Pilar; Kschonsak, Marc; Bravo, Sol; Nakane, Takanori; Rappsilber, Juri; Aragon, Luis; Beck, Martin; Löwe, Jan; Haering, Christian H.
Afiliação
  • Lee BG; MRC Laboratory of Molecular Biology, Cambridge, UK.
  • Merkel F; Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
  • Allegretti M; Collaboration for joint PhD degree between EMBL and Heidelberg University, Faculty of Biosciences, Heidelberg, Germany.
  • Hassler M; Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
  • Cawood C; Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
  • Lecomte L; Biocenter, Julius-Maximilians-Universität Würzburg, Würzburg, Germany.
  • O'Reilly FJ; MRC London Institute of Medical Sciences, London, UK.
  • Sinn LR; Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
  • Gutierrez-Escribano P; Collaboration for joint PhD degree between EMBL and Heidelberg University, Faculty of Biosciences, Heidelberg, Germany.
  • Kschonsak M; Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.
  • Bravo S; Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.
  • Nakane T; MRC London Institute of Medical Sciences, London, UK.
  • Rappsilber J; Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
  • Aragon L; Structural Biology, Genentech, South San Francisco, CA, USA.
  • Beck M; Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
  • Löwe J; MRC Laboratory of Molecular Biology, Cambridge, UK.
  • Haering CH; Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.
Nat Struct Mol Biol ; 27(8): 743-751, 2020 08.
Article em En | MEDLINE | ID: mdl-32661420
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Proteínas Nucleares / Proteínas Cromossômicas não Histona / Proteínas de Transporte / Proteínas de Saccharomyces cerevisiae Idioma: En Revista: Nat Struct Mol Biol Ano de publicação: 2020 Tipo de documento: Article
Texto completo
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XML
PubMed Links
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Proteínas Nucleares / Proteínas Cromossômicas não Histona / Proteínas de Transporte / Proteínas de Saccharomyces cerevisiae Idioma: En Revista: Nat Struct Mol Biol Ano de publicação: 2020 Tipo de documento: Article